Hybridoma proteins (HP) with binding characteristics of high specificity and affinity for oligosaccharides would be invaluable reagents in the study of oligosaccharide localization, synthesis and excretion. Additionally, such antibodies might be used to purify or assess homogeneity of oligosaccharides from biological samples (of urine, plasma, tumors, etc.). High affinity characteristics of HP might be advantageously utilized for quantitative radioimmunoassays via isotope dilution techniques. Glycoconjugates of a urinary glucose-containing tetrasaccharide-Glcalpha1-6Glcalpha1-4Glcalpha1-4 Glc-linked to key-hole-limpet hemocyanin (KLH) have been used to examine the general feasibility and ease of this hybridoma approach to carbohydrate-structural analysis.